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P56716

- RP1_MOUSE

UniProt

P56716 - RP1_MOUSE

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Protein
Oxygen-regulated protein 1
Gene
Rp1, Orp1, Rp1h
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.2 Publications

GO - Molecular functioni

  1. microtubule binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. axoneme assembly Source: UniProtKB
  2. cellular response to light stimulus Source: MGI
  3. intracellular signal transduction Source: InterPro
  4. microtubule polymerization Source: BHF-UCL
  5. negative regulation of microtubule depolymerization Source: BHF-UCL
  6. photoreceptor cell development Source: UniProtKB
  7. photoreceptor cell maintenance Source: UniProtKB
  8. photoreceptor cell outer segment organization Source: UniProtKB
  9. retina development in camera-type eye Source: MGI
  10. retina morphogenesis in camera-type eye Source: MGI
  11. retinal cone cell development Source: UniProtKB
  12. retinal rod cell development Source: UniProtKB
  13. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Oxygen-regulated protein 1
Alternative name(s):
Retinitis pigmentosa RP1 protein homolog
Gene namesi
Name:Rp1
Synonyms:Orp1, Rp1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1341105. Rp1.

Subcellular locationi

Cytoplasmcytoskeletoncilium axoneme. Cell projectionciliumphotoreceptor outer segment
Note: Specifically localized in the connecting cilia of rod and cone photoreceptors.3 Publications

GO - Cellular componenti

  1. axoneme Source: UniProtKB
  2. cilium Source: MGI
  3. microtubule associated complex Source: UniProtKB
  4. photoreceptor connecting cilium Source: UniProtKB
  5. photoreceptor inner segment Source: UniProtKB
  6. photoreceptor outer segment Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

As early as postnatal day 7, mice have already undergone significant molecular retinal changes. The molecular responses change dramatically during development and were distinct from responses to the disruption of the photoreceptor transcription factors Crx, Pde6b and Nrl. The JNK signaling cascades are specifically compromised in Rp1 defective retinas. Double heterozygotes of Rp1 and Rp1l1 exhibit abnormal outer segment morphology and reduced single rod photosensitivity and dark currents.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20952095Oxygen-regulated protein 1
PRO_0000097411Add
BLAST

Proteomic databases

PaxDbiP56716.
PRIDEiP56716.

PTM databases

PhosphoSiteiP56716.

Expressioni

Tissue specificityi

Expressed in the cell bodies and inner segments of photoreceptors. Not found in liver, spleen, kidney, brain, thymus, muscle, heart, lung and testis.

Inductioni

Gene expression is stimulated by retinal hypoxia and suppressed by relative retinal hyperoxia.

Gene expression databases

BgeeiP56716.
CleanExiMM_RP1H.
GenevestigatoriP56716.

Interactioni

Subunit structurei

Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1. Interacts with MAK.3 Publications

Protein-protein interaction databases

DIPiDIP-59493N.
IntActiP56716. 1 interaction.
MINTiMINT-4132931.
STRINGi10090.ENSMUSP00000111202.

Structurei

3D structure databases

ProteinModelPortaliP56716.
SMRiP56716. Positions 34-108.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 11783Doublecortin 1
Add
BLAST
Domaini157 – 23680Doublecortin 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi655 – 6606Poly-Lys

Domaini

The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation By similarity.

Sequence similaritiesi

Contains 2 doublecortin domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG313727.
GeneTreeiENSGT00530000063898.
HOGENOMiHOG000136857.
HOVERGENiHBG018173.
OMAiEYHMFTH.
OrthoDBiEOG7N37DH.
PhylomeDBiP56716.
TreeFamiTF318770.

Family and domain databases

Gene3Di3.10.20.230. 2 hits.
InterProiIPR003533. Doublecortin_dom.
[Graphical view]
PfamiPF03607. DCX. 2 hits.
[Graphical view]
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56716-1 [UniParc]FASTAAdd to Basket

« Hide

MSDTPSTSFS MIHLTSEGQV PSPRHSNITH PVVAKRISFY KSGDPQFGGV     50
RVVVNPRSFK TFDALLDSLS RKVPLPFGVR NISTPRGRHS ITRLEELEDG 100
KSYVCSHNKK VLPVDLDKAR RRPRPWLSSR SISTHVQLCP ATANMSTMAP 150
GMLRAPRRLV VFRNGDPKNK HVVLLSRRIT QSFEAFLQYL TQVMQCPVAK 200
LYATDGRKVP SLQAVILSSG AVVAAGREPF KPGNYDIQKY LLPAKLPGIS 250
HRVHQKGKAK IEKRKMSTHM PSDLRPQTDS LISEKTYDCF SDFSVAPENY 300
LALETHESQS LSTYPSEDDV EKSIVFNQDG TMTVVMKVRF KIKEEETVKW 350
TTTVNRAGLS NNDEKNKKSS YPGKTDYGPS SLKLEACSLP EDIVDTTQQG 400
SLTEEENTQM TEQQALSCSS ASWENASMET DIQESQKQVK HFYRPPTPGP 450
RRMRQKKSVI GTVTVVSETE VQEKQFSYSE ERKGGEKSEY HMFTHSCSKM 500
SSVSNKLVQI GSDNEMESAL ERTRESGSLK SQAINAGAIE ITSQKVLKMC 550
HNNALPSTAP ENSVVEEGTD NSAVSGTATI KHFRTCGNAN DSFSSITADS 600
TPTSVNNYSN DRNISELPSV GSPVLTMRLV NEFAHCGLTE KPENRKKVLS 650
SSASKKKKKK SQQRMITSND KKKVIETKGP PNIAGKIPRA GTTAQERLLQ 700
ESDCPDKGGR VCEQGLNISP MAIESNNFFP KSNPTFSKNF YKNKLNTFQN 750
PKTQKLLAKR KSRPRKIVST ERLRKQEIGQ EDKILLHSDS KLCESHLEKQ 800
SLFHVFNILE EDQKVLHRPP FQVEKVARNL KGMAKKSLVP KVNDLHIMLR 850
NQKKQMGVKL KSGAEVSEQH VTTRADPLAS LKKPDFPEGI PHHSGKSYVK 900
RWLQNINSYP DFEHRKSGPL CQNRSDVVNY NRNGFLGNNL HTTSSKGNGF 950
LMESNKSKTK NDNWSGNTNQ ETGKSLVAKD NGEELNKHHC ESQNGSLYDS 1000
YLVSLHDNCT LSQTTINEPS TKSHLSIEKS RPEVKLVYQE MNFATKRQSI 1050
EVAIQVDTMG ENVLKDYLPA LLLRHLEAFV PNNQKHQNGI SQIPGSLAEV 1100
VFPSVIDNSS TNLLLAWLLV LNLKRTMNSF CQSDAHKMTN RPSETAALLE 1150
VLKHVAITEE ADDLKAAVAN LMESTKTCSG SSGREQDMLP VNCTASSLHS 1200
VDECNENGSA QKTLLDEGYS VMGDCTSEMV SKSCNSSCEM HMVSKTNPPK 1250
QVDDQSDGLL TSNSCTVSQR STGACFLTDG VYSHEACAQK EGVYEGACLS 1300
DETHIPIRDC HTIHSVHSKE NKCTDDLEST EELKTVDKVP KGLSILADSM 1350
YKNDSNVSTF QNVNKLSSQR TLLSKTYLDS DKDYSPLEEF QNCPRKKIVN 1400
KKKSISSDKE ESRTSEEPRS ITNSMTSSER NAISELESFE ELESQDTSIF 1450
NMNVRAEKKS TKETMQKQSE ARMSSELINV SGRKIIEQER RNTAILETTA 1500
RGQVTPPSLA FCYDSNKNTE KEISEGETKM RVKKMVDSME NESYSESSLN 1550
FKKHHRSPGT LDWSDYGSDS ESGYPCKASS NSHNDDSGQE KEPTRGIVKR 1600
AIEKLYGKAE IIKPPFFHGS IHKSQVCPYN SVEVQCAKKT NFYESECQSL 1650
VSSEQVSRSS LIFQEFPQVD ANGMGDSFGD SSIENVTKSS AHDRVFTEKE 1700
NGKLIDNGKW LLRENHLWRV SSDNPGMYGN ADTTSVDTLI DKNSIEVPYS 1750
HFGELAPGPT MAELSSSEIE EMTQPLEVKC NYFNFPHGSD SEPFGEDFPD 1800
AQNKTCPKEK IPNHHTEEKG NYPSERLCTS VTQAFVSAGN KVHPVCSDAI 1850
KTQPLPGSNI THGALQEGDS LDKLYALCGQ HCPILTVIIQ PVNEESRGFA 1900
YRKDSDIENS LDFQLWMKIY PFMPQSKKHV FRSDGRNVSV GEEFAGNVIG 1950
DLCDQLYFKS MIDLVDQRAN SLGKEINLKK FQLYLKKSFS DPLSTSLLVV 2000
ENRNSVSLSP SSWTDNFKSI DENNNFLNRL PNSSKNPNQV VRENTNFQFH 2050
LELFGQVYLL DICQVEKPLN IKTRSKLEMY YILEGEVLFI WEEEK 2095
Length:2,095
Mass (Da):234,388
Last modified:June 6, 2002 - v2
Checksum:iCA5301316633BD62
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155141 mRNA. Translation: AAD42089.2.
AF291754 Genomic DNA. Translation: AAM17919.1.
BC120927 mRNA. Translation: AAI20928.1.
BC120928 mRNA. Translation: AAI20929.1.
CCDSiCCDS14804.1.
RefSeqiNP_035413.1. NM_011283.2.
UniGeneiMm.294263.

Genome annotation databases

EnsembliENSMUST00000027032; ENSMUSP00000027032; ENSMUSG00000025900.
GeneIDi19888.
KEGGimmu:19888.
UCSCiuc007aex.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155141 mRNA. Translation: AAD42089.2 .
AF291754 Genomic DNA. Translation: AAM17919.1 .
BC120927 mRNA. Translation: AAI20928.1 .
BC120928 mRNA. Translation: AAI20929.1 .
CCDSi CCDS14804.1.
RefSeqi NP_035413.1. NM_011283.2.
UniGenei Mm.294263.

3D structure databases

ProteinModelPortali P56716.
SMRi P56716. Positions 34-108.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-59493N.
IntActi P56716. 1 interaction.
MINTi MINT-4132931.
STRINGi 10090.ENSMUSP00000111202.

PTM databases

PhosphoSitei P56716.

Proteomic databases

PaxDbi P56716.
PRIDEi P56716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027032 ; ENSMUSP00000027032 ; ENSMUSG00000025900 .
GeneIDi 19888.
KEGGi mmu:19888.
UCSCi uc007aex.2. mouse.

Organism-specific databases

CTDi 6101.
MGIi MGI:1341105. Rp1.

Phylogenomic databases

eggNOGi NOG313727.
GeneTreei ENSGT00530000063898.
HOGENOMi HOG000136857.
HOVERGENi HBG018173.
OMAi EYHMFTH.
OrthoDBi EOG7N37DH.
PhylomeDBi P56716.
TreeFami TF318770.

Miscellaneous databases

NextBioi 297400.
PROi P56716.
SOURCEi Search...

Gene expression databases

Bgeei P56716.
CleanExi MM_RP1H.
Genevestigatori P56716.

Family and domain databases

Gene3Di 3.10.20.230. 2 hits.
InterProi IPR003533. Doublecortin_dom.
[Graphical view ]
Pfami PF03607. DCX. 2 hits.
[Graphical view ]
SMARTi SM00537. DCX. 2 hits.
[Graphical view ]
PROSITEi PS50309. DC. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein cause dominant retinitis pigmentosa."
    Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.
    Nat. Genet. 22:248-254(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 67-76.
    Tissue: Retina.
  2. "Progressive photoreceptor degeneration, outer segment dysplasia, and rhodopsin mislocalization in mice with targeted disruption of the retinitis pigmentosa-1 (Rp1) gene."
    Gao J., Cheon K., Nusinowitz S., Liu Q., Bei D., Atkins K., Azimi A., Daiger S.P., Farber D.B., Heckenlively J.R., Pierce E.A., Sullivan L.S., Zuo J.
    Proc. Natl. Acad. Sci. U.S.A. 99:5698-5703(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 357-367, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Identification and subcellular localization of the RP1 protein in human and mouse photoreceptors."
    Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.
    Invest. Ophthalmol. Vis. Sci. 43:22-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein."
    Liu Q., Zuo J., Pierce E.A.
    J. Neurosci. 24:6427-6436(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  8. "Distinct gene expression profiles and reduced JNK signaling in retinitis pigmentosa caused by RP1 mutations."
    Liu J., Huang Q., Higdon J., Liu W., Xie T., Yamashita T., Cheon K., Cheng C., Zuo J.
    Hum. Mol. Genet. 14:2945-2958(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Essential and synergistic roles of RP1 and RP1L1 in rod photoreceptor axoneme and retinitis pigmentosa."
    Yamashita T., Liu J., Gao J., LeNoue S., Wang C., Kaminoh J., Bowne S.J., Sullivan L.S., Daiger S.P., Zhang K., Fitzgerald M.E., Kefalov V.J., Zuo J.
    J. Neurosci. 29:9748-9760(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RP1L1, DISRUPTION PHENOTYPE.
  10. "Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival."
    Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S., Koyasu T., Kondo M., Furukawa T.
    Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAK.

Entry informationi

Entry nameiRP1_MOUSE
AccessioniPrimary (citable) accession number: P56716
Secondary accession number(s): Q548Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 6, 2002
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi